TRM3_HCMVA
ID TRM3_HCMVA Reviewed; 674 AA.
AC P16732; Q7M6K2;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1990, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Tripartite terminase subunit 3 {ECO:0000255|HAMAP-Rule:MF_04013};
DE EC=3.1.-.- {ECO:0000255|HAMAP-Rule:MF_04013};
DE AltName: Full=Terminase large subunit {ECO:0000255|HAMAP-Rule:MF_04013};
GN Name=TRM3 {ECO:0000255|HAMAP-Rule:MF_04013}; OrderedLocusNames=UL89;
OS Human cytomegalovirus (strain AD169) (HHV-5) (Human herpesvirus 5).
OC Viruses; Duplodnaviria; Heunggongvirae; Peploviricota; Herviviricetes;
OC Herpesvirales; Herpesviridae; Betaherpesvirinae; Cytomegalovirus.
OX NCBI_TaxID=10360;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=2161319; DOI=10.1007/978-3-642-74980-3_6;
RA Chee M.S., Bankier A.T., Beck S., Bohni R., Brown C.M., Cerny R.,
RA Horsnell T., Hutchison C.A. III, Kouzarides T., Martignetti J.A.,
RA Preddie E., Satchwell S.C., Tomlinson P., Weston K.M., Barrell B.G.;
RT "Analysis of the protein-coding content of the sequence of human
RT cytomegalovirus strain AD169.";
RL Curr. Top. Microbiol. Immunol. 154:125-169(1990).
RN [2]
RP GENOME REANNOTATION.
RX PubMed=12533697; DOI=10.1099/vir.0.18606-0;
RA Davison A.J., Dolan A., Akter P., Addison C., Dargan D.J., Alcendor D.J.,
RA McGeoch D.J., Hayward G.S.;
RT "The human cytomegalovirus genome revisited: comparison with the chimpanzee
RT cytomegalovirus genome.";
RL J. Gen. Virol. 84:17-28(2003).
RN [3]
RP ERRATUM OF PUBMED:12533697.
RA Davison A.J., Dolan A., Akter P., Addison C., Dargan D.J., Alcendor D.J.,
RA McGeoch D.J., Hayward G.S.;
RL J. Gen. Virol. 84:1053-1053(2003).
RN [4]
RP IDENTIFICATION.
RX PubMed=15452216; DOI=10.1128/jvi.78.20.10960-10966.2004;
RA Varnum S.M., Streblow D.N., Monroe M.E., Smith P., Auberry K.J.,
RA Pasa-Tolic L., Wang D., Camp D.G. II, Rodland K., Wiley S., Britt W.,
RA Shenk T., Smith R.D., Nelson J.A.;
RT "Identification of proteins in human cytomegalovirus (HCMV) particles: the
RT HCMV proteome.";
RL J. Virol. 78:10960-10966(2004).
RN [5]
RP ERRATUM OF PUBMED:15452216.
RA Varnum S.M., Streblow D.N., Monroe M.E., Smith P., Auberry K.J.,
RA Pasa-Tolic L., Wang D., Camp D.G. II, Rodland K., Wiley S., Britt W.,
RA Shenk T., Smith R.D., Nelson J.A.;
RL J. Virol. 78:13395-13395(2004).
RN [6]
RP REGION, AND INTERACTION WITH UL56.
RX PubMed=16846228; DOI=10.1021/bi0600796;
RA Thoma C., Borst E., Messerle M., Rieger M., Hwang J.S., Bogner E.;
RT "Identification of the interaction domain of the small terminase subunit
RT pUL89 with the large subunit pUL56 of human cytomegalovirus.";
RL Biochemistry 45:8855-8863(2006).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 418-674.
RX PubMed=20805464; DOI=10.1073/pnas.1007144107;
RA Nadal M., Mas P.J., Blanco A.G., Arnan C., Sola M., Hart D.J., Coll M.;
RT "Structure and inhibition of herpesvirus DNA packaging terminase nuclease
RT domain.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:16078-16083(2010).
CC -!- FUNCTION: Component of the molecular motor that translocates viral
CC genomic DNA in empty capsid during DNA packaging. Forms a tripartite
CC terminase complex together with TRM1 and TRM2 in the host cytoplasm.
CC Once the complex reaches the host nucleus, it interacts with the capsid
CC portal vertex. This portal forms a ring in which genomic DNA is
CC translocated into the capsid. TRM3 carries an RNase H-like nuclease
CC activity that plays an important role for the cleavage of concatemeric
CC viral DNA into unit length genomes. {ECO:0000255|HAMAP-Rule:MF_04013}.
CC -!- SUBUNIT: Interacts with the terminase subunits TRM1 and TRM2. Interacts
CC with portal protein. {ECO:0000255|HAMAP-Rule:MF_04013,
CC ECO:0000269|PubMed:16846228}.
CC -!- SUBCELLULAR LOCATION: Host nucleus {ECO:0000255|HAMAP-Rule:MF_04013}.
CC Note=Responsible for the nuclear localization of the two others
CC subunits TRM1 and TRM2. {ECO:0000255|HAMAP-Rule:MF_04013}.
CC -!- SIMILARITY: Belongs to the herpesviridae TRM3 protein family.
CC {ECO:0000255|HAMAP-Rule:MF_04013}.
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DR EMBL; X17403; CAA35363.1; -; Genomic_DNA.
DR EMBL; BK000394; DAA00186.1; -; Genomic_DNA.
DR PIR; S09853; QQBEI5.
DR PDB; 3N4P; X-ray; 2.15 A; A/B/C/D=418-674.
DR PDB; 3N4Q; X-ray; 3.20 A; A/B/C/D=418-674.
DR PDB; 6EY7; X-ray; 2.90 A; A/B/C/D=400-674.
DR PDBsum; 3N4P; -.
DR PDBsum; 3N4Q; -.
DR PDBsum; 6EY7; -.
DR BMRB; P16732; -.
DR SMR; P16732; -.
DR ChEMBL; CHEMBL3991482; -.
DR EvolutionaryTrace; P16732; -.
DR Proteomes; UP000008991; Genome.
DR Proteomes; UP000008992; Genome.
DR GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0004518; F:nuclease activity; IEA:UniProtKB-UniRule.
DR GO; GO:0051276; P:chromosome organization; IEA:InterPro.
DR GO; GO:0019076; P:viral release from host cell; IEA:UniProtKB-UniRule.
DR Gene3D; 3.30.420.320; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_04013; HSV_TRM3; 1.
DR InterPro; IPR003498; DNA_pack_C.
DR InterPro; IPR038435; DNA_pack_C_sf.
DR InterPro; IPR003499; DNA_pack_N.
DR InterPro; IPR033663; HSV_TRM3.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF02499; DNA_pack_C; 1.
DR Pfam; PF02500; DNA_pack_N; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 1: Evidence at protein level;
KW 3D-structure; DNA-binding; Host nucleus; Hydrolase; Reference proteome;
KW Viral genome packaging; Viral release from host cell.
FT CHAIN 1..674
FT /note="Tripartite terminase subunit 3"
FT /id="PRO_0000115947"
FT REGION 580..600
FT /note="Required for interaction with UL56 and DNA
FT packaging"
FT /evidence="ECO:0000269|PubMed:16846228"
FT MOTIF 212..219
FT /note="Walker A motif"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04013"
FT MOTIF 305..310
FT /note="Walker B motif"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04013"
FT ACT_SITE 310
FT /note="For ATPase activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04013"
FT ACT_SITE 463
FT /note="For nuclease activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04013"
FT ACT_SITE 534
FT /note="For nuclease activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04013"
FT ACT_SITE 651
FT /note="For nuclease activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04013"
FT HELIX 432..440
FT /evidence="ECO:0007829|PDB:3N4P"
FT STRAND 441..443
FT /evidence="ECO:0007829|PDB:3N4P"
FT HELIX 445..447
FT /evidence="ECO:0007829|PDB:3N4P"
FT HELIX 448..453
FT /evidence="ECO:0007829|PDB:6EY7"
FT STRAND 457..463
FT /evidence="ECO:0007829|PDB:3N4P"
FT STRAND 468..470
FT /evidence="ECO:0007829|PDB:3N4P"
FT STRAND 475..483
FT /evidence="ECO:0007829|PDB:3N4P"
FT STRAND 486..495
FT /evidence="ECO:0007829|PDB:3N4P"
FT HELIX 504..522
FT /evidence="ECO:0007829|PDB:3N4P"
FT STRAND 528..534
FT /evidence="ECO:0007829|PDB:3N4P"
FT HELIX 539..556
FT /evidence="ECO:0007829|PDB:3N4P"
FT STRAND 560..564
FT /evidence="ECO:0007829|PDB:3N4P"
FT STRAND 566..568
FT /evidence="ECO:0007829|PDB:3N4P"
FT TURN 569..571
FT /evidence="ECO:0007829|PDB:3N4P"
FT STRAND 572..575
FT /evidence="ECO:0007829|PDB:3N4P"
FT HELIX 582..595
FT /evidence="ECO:0007829|PDB:3N4P"
FT STRAND 599..606
FT /evidence="ECO:0007829|PDB:3N4P"
FT STRAND 608..611
FT /evidence="ECO:0007829|PDB:3N4P"
FT STRAND 612..614
FT /evidence="ECO:0007829|PDB:6EY7"
FT HELIX 616..625
FT /evidence="ECO:0007829|PDB:3N4P"
FT HELIX 651..661
FT /evidence="ECO:0007829|PDB:3N4P"
FT HELIX 665..670
FT /evidence="ECO:0007829|PDB:3N4P"
FT STRAND 671..673
FT /evidence="ECO:0007829|PDB:3N4Q"
SQ SEQUENCE 674 AA; 77079 MW; E73D82634C4BE739 CRC64;
MLRGDSAAKI QERYAELQKR KSHPTSCIST AFTNVATLCR KRYQMMHPEL GLAHSCNEAF
LPLMAFCGRH RDYNSPEESQ RELLFHERLK SALDKLTFRP CSEEQRASYQ KLDALTELYR
DPQFQQINNF MTDFKKWLDG GFSTAVEGDA KAIRLEPFQK NLLIHVIFFI AVTKIPVLAN
RVLQYLIHAF QIDFLSQTSI DIFKQKATVF LVPRRHGKTW FIIPIISFLL KHMIGISIGY
VAHQKHVSQF VLKEVEFRCR HTFARDYVVE NKDNVISIDH RGAKSTALFA SCYNTNSIRG
QNFHLLLVDE AHFIKKEAFN TILGFLAQNT TKIIFISSTN TTSDSTCFLT RLNNAPFDML
NVVSYVCEEH LHSFTEKGDA TACPCYRLHK PTFISLNSQV RKTANMFMPG AFMDEIIGGT
NKISQNTVLI TDQSREEFDI LRYSTLNTNA YDYFGKTLYV YLDPAFTTNR KASGTGVAAV
GAYRHQFLIY GLEHFFLRDL SESSEVAIAE CAAHMIISVL SLHPYLDELR IAVEGNTNQA
AAVRIACLIR QSVQSSTLIR VLFYHTPDQN HIEQPFYLMG RDKALAVEQF ISRFNSGYIK
ASQELVSYTI KLSHDPIEYL LEQIQNLHRV TLAEGTTARY SAKRQNRISD DLIIAVIMAT
YLCDDIHAIR FRVS
